ClpC | Chloroplastic form of HSP100

AS01 001  |  Clonality: Polyclonal  |  Host: Rabbit  |  Reactivity: A.thaliana, C.reinhardtii, cyanobacteria, Plectonema sp., Streptomyces sp.

ClpC | Chloroplastic form of HSP100 in the group Antibodies Plant/Algal  / Photosynthesis  / Proteases at Agrisera AB (Antibodies for research) (AS01 001)
ClpC | Chloroplastic form of HSP100


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Product name, number (Agrisera, Sweden)

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Product Information


Recombinant ClpC (C-terminal domain overexpressed as fusion with maltose-binding protein), UniProt: Q55023

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 100 ĩl
Reconstitution For reconstitution add 100 ĩl of sterile water
Storage Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
Tested applications Immunoprecipitation (IP), Immunohistochemistry (IHC), Western blot (WB),
Recommended dilution 1 : 1000 (IHC), 1 : 5000 on 10 µg of total protein, (WB)
Expected | apparent MW

92 | 87 kDa


Confirmed reactivity Arabidopsis thaliana, Synechococcus sp., Chlamydomonas reinhardtii, Streptomyces sp.
Predicted reactivity

Algae (red), Catalpa bungei, Hordeum vulgare, Nicotiana tabacum, Ostreococcus sp., Oryza sativa, Populus trichocarpa,  Physcomitrium patens, Pisum sativum, Solanum tuberosum,  Zea mays

Species of your interest not listed? Contact us
Not reactive in Different strains of Mycobacterium smegmatis

Application examples

Additional information

Additional information

Anti-ClpC antibodies will also recognized Arabidopsis thaliana isoform ClpC1 (At5g50920) and ClpC2 (At3g48870).

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ClpC is a chloroplastic protein of the Hsp100 family. It is believed to function as a housekeeping enzyme, both in its capacity as an independent molecular chaperone and as the regulatory component of the Clp protease.

Product citations

Selected references Jiang et al. (2020). Plastid chaperone HSP90C guides precursor proteins to the SEC translocase for thylakoid transport. J Exp Bot. 2020 Aug 27;eraa399.doi: 10.1093/jxb/eraa399.
Lee et al. (2018). Prolines in Transit Peptides Are Crucial for Efficient Preprotein Translocation into Chloroplasts. Plant Physiol. 2018 Jan;176(1):663-677. doi: 10.1104/pp.17.01553. Epub 2017 Nov 20.
Hu et al. (2015). Site-specific Nitrosoproteomic Identification of Endogenously S-Nitrosylated Proteins in Arabidopsis. Plant Physiol. 2015 Feb 19. pii: pp.00026.2015.
Rosano et al. (2011). Insights into the Clp/HSP100 chaperone system from chloroplasts of Arabidopsis thaliana. J Biol Chem. Aug 26;286(34):29671-80. (Western blot, Arabidopsis thaliana)
Karradt et al. (2008) NblA, a Key Protein of Phycobilisome Degradation, Interacts with ClpC, a HSP100 Chaperone Partner of a Cyanobacterial Clp Protease. J Biol Chem 283: 32394-32403.
Porankiewicz & Clarke (1997) Induction of the heat shock protein ClpB affects cold acclimation in the cyanobacterium Synechococcs sp. strain PCC7942. J Bacteriol 179:5111-5117.

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